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Q8WXH0 (SYNE2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nesprin-2
Alternative name(s):
Nuclear envelope spectrin repeat protein 2
Nucleus and actin connecting element protein
Short name=Protein NUANCE
Synaptic nuclear envelope protein 2
Short name=Syne-2
Gene names
Name:SYNE2
Synonyms:KIAA1011, NUA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length6885 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Involved in the maintenance of nuclear organization and structural integrity. Connects nuclei to the cytoskeleton by interacting with the nuclear envelope and with F-actin in the cytoplasm. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for centrosome migration to the apical cell surface during early ciliogenesis. Ref.1 Ref.14 Ref.16 Ref.21

Subunit structure

Component of LINC complexes composed of SUN domain-containing proteins SUN1 or SUN2 coupled to KASH domain-containing proteins (SYNE1, SYNE2 or SYNE3), also called nesprins. Interacts with F-actin via its N-terminal domain. Interacts with EMD, LMNA and MKS3. Ref.1 Ref.13 Ref.14 Ref.16 Ref.19

Subcellular location

Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side Potential. Sarcoplasmic reticulum membrane; Single-pass type IV membrane protein Potential. Cell membrane; Single-pass membrane protein Potential. Cytoplasmcytoskeleton. Mitochondrion. Nucleusnucleoplasm. Note: Different isoform patterns are found in the different compartments of the cell. The isoforms having the C-terminal transmembrane span can be found in several organellar membranes like the nuclear envelope, the sarcoplasmic reticulum of myoblasts, or the lamellipodia and focal adhesions at the cell membrane. The largest part of the outer nuclear membrane-associated protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. Remains associated with the nuclear envelope during its breakdown in mitotic cells. Shorter solubles isoforms can be found in the cytoplasm and within the nucleus. Ref.12 Ref.13 Ref.16

Tissue specificity

Widely expressed, with higher level in kidney, adult and fetal liver, stomach and placenta. Weakly expressed in skeletal muscle and brain. Isoform 5 is highly expressed in pancreas, skeletal muscle and heart. Ref.13

Domain

The KASH domain mediates the nuclear envelope targeting. Ref.14

Involvement in disease

Emery-Dreifuss muscular dystrophy 5 (EDMD5) [MIM:612999]: A degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25

Sequence similarities

Belongs to the nesprin family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 1 KASH domain.

Contains 9 spectrin repeats.

Sequence caution

The sequence BAB84881.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAB45729.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB55905.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Mitochondrion
Nucleus
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Emery-Dreifuss muscular dystrophy
   DomainCoiled coil
Repeat
Transmembrane
Transmembrane helix
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcentrosome localization

Inferred from mutant phenotype Ref.21. Source: UniProtKB

cytoskeletal anchoring at nuclear membrane

Inferred from direct assay Ref.14. Source: UniProtKB

establishment or maintenance of cell polarity

Inferred from electronic annotation. Source: Compara

fibroblast migration

Inferred from electronic annotation. Source: Compara

nuclear envelope organization

Inferred from electronic annotation. Source: Compara

nuclear migration along microfilament

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to nucleus

Inferred from electronic annotation. Source: Compara

   Cellular_componentSUN-KASH complex

Inferred from direct assay Ref.14. Source: UniProtKB

Z disc

Inferred from direct assay Ref.13. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

filopodium membrane

Inferred from direct assay Ref.13. Source: UniProtKB

focal adhesion

Inferred from direct assay Ref.13. Source: UniProtKB

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lamellipodium membrane

Inferred from direct assay Ref.13. Source: UniProtKB

mitochondrial part

Inferred from direct assay Ref.13. Source: UniProtKB

nuclear lumen

Inferred from direct assay Ref.13. Source: UniProtKB

nuclear membrane

Inferred from direct assay. Source: HPA

nuclear outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcoplasmic reticulum

Inferred from direct assay Ref.13. Source: UniProtKB

sarcoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionactin binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WXH0-1)

Also known as: Nesprin-2 Giant; NUANCE;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8WXH0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     6444-6444: S → SDVEIPENPEAYLKMTTKTLKASS
     6801-6801: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8WXH0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6030: Missing.
Note: Produced by exon skipping that results in a frameshift. No experimental confirmation available.
Isoform 4 (identifier: Q8WXH0-4)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-6122: Missing.
Isoform 5 (identifier: Q8WXH0-5)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1-6366: Missing.
     6444-6444: S → SDVEIPENPEAYLKMTTKTLKASS
     6664-6664: Q → QGSKTRPRSDVLFFK
Isoform 6 (identifier: Q8WXH0-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6469: Missing.
     6664-6664: Q → QGSKTRPRSDVLFFK
     6801-6801: Missing.
Isoform 7 (identifier: Q8WXH0-7)

Also known as: Gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3638: Missing.
     3828-3828: Q → QDSKCFRSGPRPNIYVSYYVTVIQ
Isoform 8 (identifier: Q8WXH0-8)

The sequence of this isoform differs from the canonical sequence as follows:
     263-285: DVDVVDPDEKSIMTYVAQFLQYS → DAWRSSALYRIYMPGTVSCASYL
     286-6885: Missing.
Note: No experimental confirmation available.
Isoform 9 (identifier: Q8WXH0-9)

Also known as: NUANCE-N-33;

The sequence of this isoform differs from the canonical sequence as follows:
     263-267: DVDVV → AYKNF
     268-6885: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 68856885Nesprin-2
PRO_0000163592

Regions

Topological domain1 – 68346834Cytoplasmic Potential
Transmembrane6835 – 685521Helical; Anchor for type IV membrane protein; Potential
Topological domain6856 – 688530Perinuclear space Potential
Domain1 – 286286Actin-binding
Domain31 – 136106CH 1
Domain181 – 286106CH 2
Repeat4944 – 5053110Spectrin 1
Repeat5054 – 5167114Spectrin 2
Repeat5170 – 5274105Spectrin 3
Repeat5852 – 591463Spectrin 4
Repeat5917 – 6019103Spectrin 5
Repeat6022 – 6133112Spectrin 6
Repeat6136 – 6242107Spectrin 7
Repeat6245 – 6349105Spectrin 8
Repeat6551 – 6658108Spectrin 9
Domain6826 – 688560KASH
Coiled coil233 – 25523 Potential
Coiled coil306 – 32318 Potential
Coiled coil461 – 47717 Potential
Coiled coil810 – 909100 Potential
Coiled coil941 – 97232 Potential
Coiled coil1008 – 104134 Potential
Coiled coil1194 – 122229 Potential
Coiled coil1299 – 133234 Potential
Coiled coil1462 – 149433 Potential
Coiled coil1566 – 160237 Potential
Coiled coil1658 – 170851 Potential
Coiled coil1747 – 177125 Potential
Coiled coil1782 – 180423 Potential
Coiled coil1923 – 196543 Potential
Coiled coil2007 – 203529 Potential
Coiled coil2176 – 220530 Potential
Coiled coil2282 – 236988 Potential
Coiled coil2422 – 247857 Potential
Coiled coil2589 – 265062 Potential
Coiled coil2696 – 271722 Potential
Coiled coil2802 – 283534 Potential
Coiled coil2866 – 2975110 Potential
Coiled coil3014 – 305744 Potential
Coiled coil3087 – 313246 Potential
Coiled coil3207 – 324135 Potential
Coiled coil3297 – 3428132 Potential
Coiled coil3464 – 350542 Potential
Coiled coil3553 – 358432 Potential
Coiled coil3655 – 372369 Potential
Coiled coil3778 – 379922 Potential
Coiled coil3853 – 391159 Potential
Coiled coil3971 – 406999 Potential
Coiled coil4272 – 429928 Potential
Coiled coil4307 – 433933 Potential
Coiled coil4493 – 453644 Potential
Coiled coil4636 – 470166 Potential
Coiled coil4831 – 486131 Potential
Coiled coil4911 – 494434 Potential
Coiled coil5308 – 534639 Potential
Coiled coil5428 – 544518 Potential
Coiled coil5505 – 552925 Potential
Coiled coil6697 – 677074 Potential

Amino acid modifications

Modified residue9551N6-acetyllysine Ref.18
Modified residue27811Phosphoserine Ref.20 Ref.23
Modified residue41081Phosphoserine Ref.15 Ref.17
Modified residue63611Phosphoserine Ref.20

Natural variations

Alternative sequence1 – 64696469Missing in isoform 6.
VSP_007158
Alternative sequence1 – 63666366Missing in isoform 5.
VSP_007157
Alternative sequence1 – 61226122Missing in isoform 4.
VSP_007156
Alternative sequence1 – 60306030Missing in isoform 3.
VSP_007155
Alternative sequence1 – 36383638Missing in isoform 7.
VSP_007154
Alternative sequence263 – 28523DVDVV…FLQYS → DAWRSSALYRIYMPGTVSCA SYL in isoform 8.
VSP_007161
Alternative sequence263 – 2675DVDVV → AYKNF in isoform 9.
VSP_007159
Alternative sequence268 – 68856618Missing in isoform 9.
VSP_007160
Alternative sequence286 – 68856600Missing in isoform 8.
VSP_007162
Alternative sequence38281Q → QDSKCFRSGPRPNIYVSYYV TVIQ in isoform 7.
VSP_007163
Alternative sequence64441S → SDVEIPENPEAYLKMTTKTL KASS in isoform 2 and isoform 5.
VSP_007164
Alternative sequence66641Q → QGSKTRPRSDVLFFK in isoform 5 and isoform 6.
VSP_007165
Alternative sequence68011Missing in isoform 2 and isoform 6.
VSP_007166
Natural variant81P → S.
Corresponds to variant rs2275017 [ dbSNP | Ensembl ].
VAR_027947
Natural variant4321S → R.
Corresponds to variant rs35554503 [ dbSNP | Ensembl ].
VAR_050238
Natural variant5741I → T.
Corresponds to variant rs9944035 [ dbSNP | Ensembl ].
VAR_027948
Natural variant13931R → W.
Corresponds to variant rs17751301 [ dbSNP | Ensembl ].
VAR_050239
Natural variant19691M → T. Ref.1
Corresponds to variant rs4902264 [ dbSNP | Ensembl ].
VAR_050240
Natural variant22841A → V. Ref.1
Corresponds to variant rs4027402 [ dbSNP | Ensembl ].
VAR_050241
Natural variant23471A → E.
Corresponds to variant rs34625768 [ dbSNP | Ensembl ].
VAR_050242
Natural variant23581N → S.
Corresponds to variant rs4027404 [ dbSNP | Ensembl ].
VAR_027949
Natural variant23591S → G.
Corresponds to variant rs7157465 [ dbSNP | Ensembl ].
VAR_050243
Natural variant23591S → N. Ref.1
Corresponds to variant rs4027404 [ dbSNP | Ensembl ].
VAR_050244
Natural variant23941A → T.
Corresponds to variant rs4027405 [ dbSNP | Ensembl ].
VAR_027950
Natural variant23951A → T. Ref.1
Corresponds to variant rs4027405 [ dbSNP | Ensembl ].
VAR_050245
Natural variant24901V → G.
Corresponds to variant rs34393543 [ dbSNP | Ensembl ].
VAR_050246
Natural variant25641I → V.
Corresponds to variant rs11628107 [ dbSNP | Ensembl ].
VAR_050247
Natural variant28011G → S.
Corresponds to variant rs1890908 [ dbSNP | Ensembl ].
VAR_027951
Natural variant28021S → G. Ref.1
Corresponds to variant rs1890908 [ dbSNP | Ensembl ].
VAR_050248
Natural variant29421I → V. Ref.1
Corresponds to variant rs3829767 [ dbSNP | Ensembl ].
VAR_050249
Natural variant30261E → D.
Corresponds to variant rs34843668 [ dbSNP | Ensembl ].
VAR_050250
Natural variant31301N → S.
Corresponds to variant rs11847087 [ dbSNP | Ensembl ].
VAR_050251
Natural variant32531D → H. Ref.1
Corresponds to variant rs8010911 [ dbSNP | Ensembl ].
VAR_050252
Natural variant33091H → R. Ref.1
Corresponds to variant rs8010699 [ dbSNP | Ensembl ].
VAR_050253
Natural variant35231K → Q.
Corresponds to variant rs35203186 [ dbSNP | Ensembl ].
VAR_050254
Natural variant39821N → H.
Corresponds to variant rs10137972 [ dbSNP | Ensembl ].
VAR_050255
Natural variant40411R → H.
Corresponds to variant rs17101661 [ dbSNP | Ensembl ].
VAR_050256
Natural variant49121P → A.
Corresponds to variant rs17766354 [ dbSNP | Ensembl ].
VAR_050257
Natural variant49131E → K.
Corresponds to variant rs12881815 [ dbSNP | Ensembl ].
VAR_050258
Natural variant50861H → Y.
Corresponds to variant rs2039475 [ dbSNP | Ensembl ].
VAR_050259
Natural variant51861L → M. Ref.1 Ref.7
Corresponds to variant rs10151658 [ dbSNP | Ensembl ].
VAR_050260
Natural variant55471D → N.
Corresponds to variant rs17179194 [ dbSNP | Ensembl ].
VAR_050261
Natural variant59401V → I in a breast cancer sample; somatic mutation. Ref.24
VAR_036255
Natural variant61551A → V.
Corresponds to variant rs2275014 [ dbSNP | Ensembl ].
VAR_050262
Natural variant62001Y → C in a breast cancer sample; somatic mutation. Ref.24
VAR_036256
Natural variant62111T → M in EDMD5. Ref.25
VAR_062977
Natural variant66811K → E.
Corresponds to variant rs35315070 [ dbSNP | Ensembl ].
VAR_050263
Natural variant66971R → W.
Corresponds to variant rs35700578 [ dbSNP | Ensembl ].
VAR_050264

Experimental info

Sequence conflict6681Missing Ref.3
Sequence conflict10871M → T Ref.3
Sequence conflict31151F → S in AAL33548. Ref.1
Sequence conflict31931E → G in AAL33548. Ref.1
Sequence conflict39511Q → L in AAL33802. Ref.2
Sequence conflict40011W → Q in AAN60443. Ref.3
Sequence conflict41581S → F in AAL33802. Ref.2
Sequence conflict41581S → F Ref.3
Sequence conflict42091I → T in AAL33802. Ref.2
Sequence conflict42091I → T Ref.3
Sequence conflict43271E → Q in AAL33802. Ref.2
Sequence conflict43271E → Q Ref.3
Sequence conflict44181N → K in AAL33802. Ref.2
Sequence conflict44181N → K Ref.3
Sequence conflict47131E → G in AAL33548. Ref.1
Sequence conflict47331P → S in AAL33802. Ref.2
Sequence conflict47331P → S Ref.3
Sequence conflict48071N → I in AAL33802. Ref.2
Sequence conflict48071N → I Ref.3
Sequence conflict48261S → P in AAL33802. Ref.2
Sequence conflict48261S → P Ref.3
Sequence conflict51661E → D in AAL33802. Ref.2
Sequence conflict51661E → D Ref.3
Sequence conflict56461T → A in AAL33802. Ref.2
Sequence conflict56461T → A Ref.3
Sequence conflict57271K → R in AAL33802. Ref.2
Sequence conflict57271K → R Ref.3

Secondary structure

...... 6885
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Nesprin-2 Giant) (NUANCE) [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 3D37E27B080ADBD8

FASTA6,885796,442
        10         20         30         40         50         60 
MASSPELPTE DEQGSWGIDD LHISLQAEQE DTQKKAFTCW INSQLARHTS PSVISDLFTD 

        70         80         90        100        110        120 
IKKGHVLLDL LEVLSGQQLP RDKGSNTFQC RINIEHALTF LRNRSIKLIN IHVTDIIDGN 

       130        140        150        160        170        180 
PSIILGLIWT IILHFHIEKL AQTLSCNYNQ PSLDDVSVVD SSPASSPPAK KCSKVQARWQ 

       190        200        210        220        230        240 
MSARKALLLW AQEQCATYES VNVTDFKSSW RNGMAFLAII HALRPDLIDM KSVKHRSNKD 

       250        260        270        280        290        300 
NLREAFRIAE QELKIPRLLE PEDVDVVDPD EKSIMTYVAQ FLQYSKDAPG TGEEAQGKVK 

       310        320        330        340        350        360 
DAMGWLTLQK EKLQKLLKDS ENDTYFKKYN SLLSFMESFN EEKKSFLDVL SIKRDLDELD 

       370        380        390        400        410        420 
KDHLQLREAW DGLDHQINAW KIKLNYALPP PLHQTEAWLQ EVEELMDEDL SASQDHSQAV 

       430        440        450        460        470        480 
TLIQEKMTLF KSLMDRFEHH SNILLTFENK DENHLPLVPP NKLEEMKRRI NNILEKKFIL 

       490        500        510        520        530        540 
LLEFHYYKCL VLGLVDEVKS KLDIWNIKYG SRESVELLLE DWHKFIEEKE FLARLDTSFQ 

       550        560        570        580        590        600 
KCGEIYKNLA GECQNINKQY MMVKSDVCMY RKNIYNVKST LQKVLACWAT YVENLRLLRA 

       610        620        630        640        650        660 
CFEETKKEEI KEVPFETLAQ WNLEHATLNE AGNFLVEVSN DVVGSSISKE LRRLNKRWRK 

       670        680        690        700        710        720 
LVSKTQLEMN LPLMIKKQDQ PTFDNSGNIL SKEEKATVEF STDMSVELPE NYNQNIKAGE 

       730        740        750        760        770        780 
KHEKENEEFT GQLKVAKDVE KLIGQVEIWE AEAKSVLDQD DVDTSMEESL KHLIAKGSMF 

       790        800        810        820        830        840 
DELMARSEDM LQMDIQNISS QESFQHVLTT GLQAKIQEAK EKVQINVVKL IAALKNLTDV 

       850        860        870        880        890        900 
SPDLDIRLKM EESQKELESY MMRAQQLLGQ RESPGELISK HKEALIISNT KSLAKYLKAV 

       910        920        930        940        950        960 
EELKNNVTED IKMSLEEKSR DVCAKWESLH HELSLYVQQL KIDIEKGKLS DNILKLEKQI 

       970        980        990       1000       1010       1020 
NKEKKLIRRG RTKGLIKEHE ACFSEEGCLY QLNHHMEVLR ELCEELPSQK SQQEVKRLLK 

      1030       1040       1050       1060       1070       1080 
DYEQKIERLL KCASEIHMTL QPTAGGTSKN EGTITTSENR GGDPHSEAPF AKSDNQPSTE 

      1090       1100       1110       1120       1130       1140 
KAMEPTMKFS LASVLRPLQE ESIMEKDYSA SINSLLERYD TYRDILEHHL QNNKFRITSD 

      1150       1160       1170       1180       1190       1200 
FSSEEDRSSS CLQAKLTDLQ VIKNETDARW KEFEIISLKL ENHVNDIKKP FVIKERDTLK 

      1210       1220       1230       1240       1250       1260 
ERERELQMTL NTRMESLETA LRLVLPVEKA SLLLCGSDLP LHKMAIQGFH LIDADRIYQH 

      1270       1280       1290       1300       1310       1320 
LRNIQDSIAK QIEICNRLEE PGNFVLKELH PFDLHAMQNI ILKYKTQFEG MNHRVQRSED 

      1330       1340       1350       1360       1370       1380 
TLKALEDFLA SLRTAKLSAE PVTDLSASDT QVAQENTLTV KNKEGEIHLM KDKAKHLDKC 

      1390       1400       1410       1420       1430       1440 
LKMLDMSFKD AERGDDTSCE NLLDAFSIKL SETHGYGVQE EFTEENKLLE ACIFKNNELL 

      1450       1460       1470       1480       1490       1500 
KNIQDVQSQI SKIGLKDPTV PAVKHRKKSL IRLDKVLDEY EEEKRHLQEM ANSLPHFKDG 

      1510       1520       1530       1540       1550       1560 
REKTVNQQCQ NTVVLWENTK ALVTECLEQC GRVLELLKQY QNFKSILTTL IQKEESVISL 

      1570       1580       1590       1600       1610       1620 
QASYMGKENL KKRIAEIEIV KEEFNEHLEV VDKINQVCKN LQFYLNKMKT FEEPPFEKEA 

      1630       1640       1650       1660       1670       1680 
NIIVDRWLDI NEKTEDYYEN LGRALALWDK LFNLKNVIDE WTEKALQKME LHQLTEEDRE 

      1690       1700       1710       1720       1730       1740 
RLKEELQVHE QKTSEFSRRV AEIQFLLQSS EIPLELQVME SSILNKMEHV QKCLTGESNC 

      1750       1760       1770       1780       1790       1800 
HALSGSTAEL REDLDQAKTQ IGMTESLLKA LSPSDSLEIF TKLEEIQQQI LQQKHSMILL 

      1810       1820       1830       1840       1850       1860 
ENQIGCLTPE LSELKKQYES VSDLFNTKKS VLQDHFSKLL NDQCKNFNDW FSNIKVNLKE 

      1870       1880       1890       1900       1910       1920 
CFESSETKKS VEQKLQKLSD FLTLEGRNSK IKQVDSVLKH VKKHLPKAHV KELISWLVGQ 

      1930       1940       1950       1960       1970       1980 
EFELEKMESI CQARAKELED SLQQLLRLQD DHRNLRKWLT NQEEKWKGME EPGEKTELFC 

      1990       2000       2010       2020       2030       2040 
QALARKREQF ESVAQLNNSL KEYGFTEEEE IIMEATCLMD RYQTLLRQLS EIEEEDKLLP 

      2050       2060       2070       2080       2090       2100 
TEDQSFNDLA HDVIHWIKEI KESLMVLNSS EGKMPLEERI QKIKEIILLK PEGDARIETI 

      2110       2120       2130       2140       2150       2160 
MKQAESSEAP LVQKTLTDIS NQWDNTLHLA STYLSHQEKL LLEGEKYLQS KEDLRLMLIE 

      2170       2180       2190       2200       2210       2220 
LKKKQEAGFA LQHGLQEKKA QLKIYKKFLK KAQDLTSLLK ELKSQGNYLL ECTKNPSFSE 

      2230       2240       2250       2260       2270       2280 
EPWLEIKHLH ESLLQQLQDS VQNLDGHVRE HDSYQVCVTD LNTTLDNFSK EFVSFSDKPV 

      2290       2300       2310       2320       2330       2340 
DQIAVEEKLQ KLQELENRLS LQDGTLKKIL ALAKSVKQNT SSVGQKIIKD DIKSLQCKQK 

      2350       2360       2370       2380       2390       2400 
DLENRLASAK QEMECCLNSI LKSKRSTEKK GKFTLPGREK QATSDVQEST QESAAVEKLE 

      2410       2420       2430       2440       2450       2460 
EDWEINKDSA VEMAMSKQLS LNAQESMKNT EDERKVNELQ NQPLELDTML RNEQLEEIEK 

      2470       2480       2490       2500       2510       2520 
LYTQLEAKKA AIKPLEQTEC LNKTETGALV LHNIGYSAQH LDNLLQALIT LKKNKESQYC 

      2530       2540       2550       2560       2570       2580 
VLRDFQEYLA AVESSMKALL TDKESLKVGP LDSVTYLDKI KKFIASIEKE KDSLGNLKIK 

      2590       2600       2610       2620       2630       2640 
WENLSNHVTD MDKKLLESQI KQLEHGWEQV EQQIQKKYSQ QVVEYDEFTT LMNKVQDTEI 

      2650       2660       2670       2680       2690       2700 
SLQQQQQHLQ LRLKSPEERA GNQSMIALTT DLQATKHGFS VLKGQAELQM KRIWGEKEKK 

      2710       2720       2730       2740       2750       2760 
NLEDGINNLK KQWETLEPLH LEAENQIKKC DIRNKMKETI LWAKNLLGEL NPSIPLLPDD 

      2770       2780       2790       2800       2810       2820 
ILSQIRKCKV THDGILARQQ SVESLAEEVK DKVPSLTTYE GSDLNNTLED LRNQYQMLVL 

      2830       2840       2850       2860       2870       2880 
KSTQRSQQLE FKLEERSNFF AIIRKFQLMV QESETLIIPR VETAATEAEL KHHHVTLEAS 

      2890       2900       2910       2920       2930       2940 
QKELQEIDSG ISTHLQELTN IYEELNVFER LFLEDQLKNL KIRTNRIQRF IQNTCNEVEH 

      2950       2960       2970       2980       2990       3000 
KIKFCRQFHE KTSALQEEAD SIQRNELLLN QEVNKGVKEE IYNLKDRLTA IKCCILQVLK 

      3010       3020       3030       3040       3050       3060 
LKKVFDYIGL NWDFSQLDQL QTQVFEKEKE LEEKIKQLDT FEEEHGKYQA LLSKMRAIDL 

      3070       3080       3090       3100       3110       3120 
QIKKMTEVVL KAPDSSPESR RLNAQILSQR IEKAKCLCDE IIKKLNENKT FDDSFKEKEI 

      3130       3140       3150       3160       3170       3180 
LQIKLNAEEN DKLYKVLQNM VLELSPKELD EKNCQDKLET SLHVLNQIKS QLQQPLLINL 

      3190       3200       3210       3220       3230       3240 
EIKHIQNEKD NCEAFQEQVW AEMCSIKAVT AIEKQREENS SEASDVETKL REFEDLQMQL 

      3250       3260       3270       3280       3290       3300 
NTSIDLRTNV LNDAYENLTR YKEAVTRAVE SITSLEAIII PYRVDVGNPE ESLEMPLRKQ 

      3310       3320       3330       3340       3350       3360 
EELESTVAHI QDLTEKLGMI SSPEAKLQLQ YTLQELVSKN SAMKEAFKAQ ETEAERYLEN 

      3370       3380       3390       3400       3410       3420 
YKCYRKMEED IYTNLSKMET VLGQSMSSLP LSYREALERL EQSKALVSNL ISTKEELMKL 

      3430       3440       3450       3460       3470       3480 
RQILRLLRLR CTENDGICLL KIVSALWEKW LSLLEAAKEW EMWCEELKQE WKFVSEEIER 

      3490       3500       3510       3520       3530       3540 
EAIILDNLQE ELPEISKTKE AATTEELSEL LDCLCQYGEN VEKQQLLLTL LLQRIRSIQN 

      3550       3560       3570       3580       3590       3600 
VPESSGAVET VPAFQEITSM KERCNKLLQK VQKNKELVQT EIQERHSFTK EIIALKNFFQ 

      3610       3620       3630       3640       3650       3660 
QTTTSFQNMA FQDHPEKSEQ FEELQSILKK GKLTFENIME KLRIKYSEMY TIVPAEIESQ 

      3670       3680       3690       3700       3710       3720 
VEECRKALED IDEKISNEVL KSSPSYAMRR KIEEINNGLH NVEKMLQQKS KNIEKAQEIQ 

      3730       3740       3750       3760       3770       3780 
KKMWDELDLW HSKLNELDSE VQDIVEQDPG QAQEWMDNLM IPFQQYQQVS QRAECRTSQL 

      3790       3800       3810       3820       3830       3840 
NKATVKMEEY SDLLKSTEAW IENTSHLLAN PADYDSLRTL SHHASTVQMA LEDSEQKHNL 

      3850       3860       3870       3880       3890       3900 
LHSIFMDLED LSIIFETDEL TQSIQELSNQ VTALQQKIME SLPQIQRMAD DVVAIESEVK 

      3910       3920       3930       3940       3950       3960 
SMEKRVSKIK TILLSKEIFD FSPEEHLKHG EVILENIRPM KKTIAEIVSY QVELRLPQTG 

      3970       3980       3990       4000       4010       4020 
MKPLPVFQRT NQLLQDIKLL ENVTQEQNEL LKVVIKQTNE WDEEIENLKQ ILNNYSAQFS 

      4030       4040       4050       4060       4070       4080 
LEHMSPDQAD KLPQLQGEIE RMEKQILSLN QRKEDLLVDL KATVLNLHQH LKQEQEGVER 

      4090       4100       4110       4120       4130       4140 
DRLPAVTSEE GGVAERDASE RKLNRRGSMS YLAAVEEEVE ESSVKSDNGD EKAEPSPQSW 

      4150       4160       4170       4180       4190       4200 
SSLWKHDKDM EEDRASSSSG TIVQEAYGKI STSDNSMAQI LTPDSLNTEQ GPECSLRPNQ 

      4210       4220       4230       4240       4250       4260 
TEEGTTPPIE ADTLDSSDAQ GGLEPRVEKT RPEPTEVLHA CKTQVAELEL WLQQANVAVE 

      4270       4280       4290       4300       4310       4320 
PETLNADMQQ VLEQQLVGCQ AMLTEIEHKV AFLLETCKDQ GLGDNGATQH EAEALSLKLK 

      4330       4340       4350       4360       4370       4380 
TVKCNLEKVQ MMLQEKHSED QHPTILKKSS EPEHQEALQP VNLSELESIV TERPQFSRQK 

      4390       4400       4410       4420       4430       4440 
DFQQQQVLEL KPMEQKDFIK FIEFNAKKMW PQYCQHDNDT TQESSASNQA SSPENDVPDS 

      4450       4460       4470       4480       4490       4500 
ILSPQGQNGD KWQYLHHELS SKIKLPLPQL VEPQVSTNMG ILPSVTMYNF RYPTTEELKT 

      4510       4520       4530       4540       4550       4560 
YTTQLEDLRQ EASNLQTQEN MTEEAYINLD KKLFELFLTL SQCLSSVEEM LEMPRLYRED 

      4570       4580       4590       4600       4610       4620 
GSGQQVHYET LALELKKLYL ALSDKKGDLL KAMTWPGENT NLLLECFDNL QVCLEHTQAA 

      4630       4640       4650       4660       4670       4680 
AVCRSKSLKA GLDYNRSYQN EIKRLYHQLI KSKTSLQQSL NEISGQSVAE QLQKADAYTV 

      4690       4700       4710       4720       4730       4740 
ELENAESRVA KLRDEGERLH LPYALLQEVY KLEDVLDSMW GMLRARYTEL SSPFVTESQQ 

      4750       4760       4770       4780       4790       4800 
DALLQGMVEL VKIGKEKLAH GHLKQTKSKV ALQAQIENHK VFFQKLVADM LLIQAYSAKI 

      4810       4820       4830       4840       4850       4860 
LPSLLQNRET FWAEQVTEVK ILEEKSRQCG MKLQSLLQKW EEFDENYASL EKDLEILIST 

      4870       4880       4890       4900       4910       4920 
LPSVSLVEET EERLVERISF YQQIKRNIGG KHARLYQTLN EGKQLVASVS CPELEGQIAK 

      4930       4940       4950       4960       4970       4980 
LEEQWLSLNK KIDHELHRLQ ALLKHLLSYN RDSDQLTKWL ESSQHTLNYW KEQSLNVSQD 

      4990       5000       5010       5020       5030       5040 
LDTIRSNINN FFEFSKEVDE KSSLKTAVIS IGNQLLHLKE TDTATLRASL AQFEQKWTML 

      5050       5060       5070       5080       5090       5100 
ITQLPDIQEK LHQLQMEKLP SRKAITEMIS WMNNVEHQTS DEDSVHSPSS ASQVKHLLQK 

      5110       5120       5130       5140       5150       5160 
HKEFRMEMDY KQWIVDFVNQ SLLQLSTCDV ESKRYERTEF AEHLGEMNRQ WHRVHGMLNR 

      5170       5180       5190       5200       5210       5220 
KIQHLEQLLE SITESENKIQ ILNNWLEAQE ERLKTLQKPE SVISVQKLLL DCQDIENQLA 

      5230       5240       5250       5260       5270       5280 
IKSKALDELK QSYLTLESGA VPLLEDTASR IDELFQKRSS VLTQVNQLKT SMQSVLQEWK 

      5290       5300       5310       5320       5330       5340 
IYDQLYDEVN MMTIRFWYCM EHSKPVVLSL ETLRCQVENL QSLQDEAESS EGSWEKLQEV 

      5350       5360       5370       5380       5390       5400 
IGKLKGLCPS VAEIIEEKCQ NTHKRWTQVN QAIADQLQKA QSLLQLWKAY SNAHGEAAAR 

      5410       5420       5430       5440       5450       5460 
LKQQEAKFQQ LANISMSGNN LAEILPPALQ DIKELQHDVQ KTKEAFLQNS SVLDRLPQPA 

      5470       5480       5490       5500       5510       5520 
ESSTHMLLPG PLHSLQRAAY LEKMLLVKAN EFEFVLSQFK DFGVRLESLK GLIMHEEENL 

      5530       5540       5550       5560       5570       5580 
DRLHQQEKEN PDSFLNHVLA LTAQSPDIEH LNEVSLKLPL SDVAVKTLQN MNRQWIRATA 

      5590       5600       5610       5620       5630       5640 
TALERCSELQ GIGLNEKFLY CCEKWIQLLE KIEEALKVDV ANSLPELLEQ QKTYKMLEAE 

      5650       5660       5670       5680       5690       5700 
VSINQTIADS YVTQSLQLLD TTEIENRPEF ITEFSKLTDR WQNAVQGVRQ RKGDVDGLVR 

      5710       5720       5730       5740       5750       5760 
QWQDFTTSVE NLFRFLTDTS HLLSAVKGQE RFSLYQTRSL IHELKNKEIH FQRRRTTCAL 

      5770       5780       5790       5800       5810       5820 
TLEAGEKLLL TTDLKTKESV GRRISQLQDS WKDMEPQLAE MIKQFQSTVE TWDQCEKKIK 

      5830       5840       5850       5860       5870       5880 
ELKSRLQVLK AQSEDPLPEL HEDLHNEKEL IKELEQSLAS WTQNLKELQT MKADLTRHVL 

      5890       5900       5910       5920       5930       5940 
VEDVMVLKEQ IEHLHRQWED LCLRVAIRKQ EIEDRLNTWV VFNEKNKELC AWLVQMENKV 

      5950       5960       5970       5980       5990       6000 
LQTADISIEE MIEKLQKDCM EEINLFSENK LQLKQMGDQL IKASNKSRAA EIDDKLNKIN 

      6010       6020       6030       6040       6050       6060 
DRWQHLFDVI GSRVKKLKET FAFIQQLDKN MSNLRTWLAR IESELSKPVV YDVCDDQEIQ 

      6070       6080       6090       6100       6110       6120 
KRLAEQQDLQ RDIEQHSAGV ESVFNICDVL LHDSDACANE TECDSIQQTT RSLDRRWRNI 

      6130       6140       6150       6160       6170       6180 
CAMSMERRMK IEETWRLWQK FLDDYSRFED WLKSAERTAA CPNSSEVLYT SAKEELKRFE 

      6190       6200       6210       6220       6230       6240 
AFQRQIHERL TQLELINKQY RRLARENRTD TASRLKQMVH EGNQRWDNLQ RRVTAVLRRL 

      6250       6260       6270       6280       6290       6300 
RHFTNQREEF EGTRESILVW LTEMDLQLTN VEHFSESDAD DKMRQLNGFQ QEITLNTNKI 

      6310       6320       6330       6340       6350       6360 
DQLIVFGEQL IQKSEPLDAV LIEDELEELH RYCQEVFGRV SRFHRRLTSC TPGLEDEKEA 

      6370       6380       6390       6400       6410       6420 
SENETDMEDP REIQTDSWRK RGESEEPSSP QSLCHLVAPG HERSGCETPV SVDSIPLEWD 

      6430       6440       6450       6460       6470       6480 
HTGDVGGSSS HEEDEEGPYY SALSGKSISD GHSWHVPDSP SCPEHHYKQM EGDRNVPPVP 

      6490       6500       6510       6520       6530       6540 
PASSTPYKPP YGKLLLPPGT DGGKEGPRVL NGNPQQEDGG LAGITEQQSG AFDRWEMIQA 

      6550       6560       6570       6580       6590       6600 
QELHNKLKIK QNLQQLNSDI SAITTWLKKT EAELEMLKMA KPPSDIQEIE LRVKRLQEIL 

      6610       6620       6630       6640       6650       6660 
KAFDTYKALV VSVNVSSKEF LQTESPESTE LQSRLRQLSL LWEAAQGAVD SWRGGLRQSL 

      6670       6680       6690       6700       6710       6720 
MQCQDFHQLS QNLLLWLASA KNRRQKAHVT DPKADPRALL ECRRELMQLE KELVERQPQV 

      6730       6740       6750       6760       6770       6780 
DMLQEISNSL LIKGHGEDCI EAEEKVHVIE KKLKQLREQV SQDLMALQGT QNPASPLPSF 

      6790       6800       6810       6820       6830       6840 
DEVDSGDQPP ATSVPAPRAK QFRAVRTTEG EEETESRVPG STRPQRSFLS RVVRAALPLQ 

      6850       6860       6870       6880 
LLLLLLLLLA CLLPSSEEDY SCTQANNFAR SFYPMLRYTN GPPPT 

« Hide

Isoform 2 [UniParc].

Checksum: 7E7F66AF95A99F70
Show »

FASTA6,907798,862
Isoform 3 [UniParc].

Checksum: 554952A1E70DF621
Show »

FASTA85598,039
Isoform 4 (Beta) [UniParc].

Checksum: CAE53C333FE028A0
Show »

FASTA76387,403
Isoform 5 (Alpha) [UniParc].

Checksum: FA2F772713B7A977
Show »

FASTA55662,199
Isoform 6 [UniParc].

Checksum: 8BF416B8EEA07C63
Show »

FASTA42948,159
Isoform 7 (Gamma) [UniParc].

Checksum: 5F53FE3B7E37EDAB
Show »

FASTA3,270377,193
Isoform 8 [UniParc].

Checksum: A0DDB990EFD42352
Show »

FASTA28532,239
Isoform 9 (NUANCE-N-33) [UniParc].

Checksum: 0683CC937EBD8A92
Show »

FASTA26730,270

References

« Hide 'large scale' references
[1]"NUANCE, a giant protein connecting the nucleus and actin cytoskeleton."
Zhen Y.-Y., Libotte T., Munck M., Noegel A.A., Korenbaum E.
J. Cell Sci. 115:3207-3222(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 9), FUNCTION, CHARACTERIZATION, INTERACTION WITH F-ACTIN, VARIANTS THR-1969; VAL-2284; ASN-2359; THR-2395; GLY-2802; VAL-2942; HIS-3253; ARG-3309 AND MET-5186.
[2]"Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues."
Zhang Q., Skepper J.N., Yang F., Davies J.D., Hegyi L., Roberts R.G., Weissberg P.L., Ellis J.A., Shanahan C.M.
J. Cell Sci. 114:4485-4498(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 7).
[3]"The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300."
Zhang Q., Ragnauth C., Greener M.J., Shanahan C.M., Roberts R.G.
Genomics 80:473-481(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
Tissue: Testis.
[5]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
Tissue: Brain.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-956 AND 5133-6885, VARIANT MET-5186.
Tissue: Spleen and Tongue.
[8]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3367-6885 (ISOFORM 2).
Tissue: Brain.
[9]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[10]Ohara O., Nagase T., Kikuno R.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[11]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5754-6885.
[12]"Nuclear membrane proteins with potential disease links found by subtractive proteomics."
Schirmer E.C., Florens L., Guan T., Yates J.R. III, Gerace L.
Science 301:1380-1382(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[13]"Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle."
Zhang Q., Ragnauth C.D., Skepper J.N., Worth N.F., Warren D.T., Roberts R.G., Weissberg P.L., Ellis J.A., Shanahan C.M.
J. Cell Sci. 118:673-687(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH EMD AND LMNA.
[14]"Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness."
Stewart-Hutchinson P.J., Hale C.M., Wirtz D., Hodzic D.
Exp. Cell Res. 314:1892-1905(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN, INTERACTION WITH SUN1 AND SUN2.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4108, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[16]"Nesprin-2 interacts with meckelin and mediates ciliogenesis via remodelling of the actin cytoskeleton."
Dawe H.R., Adams M., Wheway G., Szymanska K., Logan C.V., Noegel A.A., Gull K., Johnson C.A.
J. Cell Sci. 122:2716-2726(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MKS3, FUNCTION.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4108, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[18]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-955, MASS SPECTROMETRY.
[19]"Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes."
Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M., Shackleton S.
J. Biol. Chem. 285:3487-3498(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUN1 AND SUN2.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2781 AND SER-6361, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[21]"Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement."
Luxton G.W., Gomes E.R., Folker E.S., Vintinner E., Gundersen G.G.
Science 329:956-959(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2781, MASS SPECTROMETRY.
[24]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-5940 AND CYS-6200.
[25]"Nesprin-1 and -2 are involved in the pathogenesis of Emery Dreifuss muscular dystrophy and are critical for nuclear envelope integrity."
Zhang Q., Bethmann C., Worth N.F., Davies J.D., Wasner C., Feuer A., Ragnauth C.D., Yi Q., Mellad J.A., Warren D.T., Wheeler M.A., Ellis J.A., Skepper J.N., Vorgerd M., Schlotter-Weigel B., Weissberg P.L., Roberts R.G., Wehnert M., Shanahan C.M.
Hum. Mol. Genet. 16:2816-2833(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDMD5 MET-6211.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF435010 mRNA. Translation: AAL33547.1.
AF435011 mRNA. Translation: AAL33548.1.
AY061757 mRNA. Translation: AAL33800.1.
AY061758 mRNA. Translation: AAL33801.1.
AY061759 mRNA. Translation: AAL33802.1.
AY184204 mRNA. Translation: AAO27772.1.
AF495911 mRNA. Translation: AAN60443.1.
AL117404 mRNA. Translation: CAB55905.2. Different initiation.
AL162832 Genomic DNA. No translation available.
AL355094 Genomic DNA. No translation available.
AL359235 Genomic DNA. No translation available.
BC042134 mRNA. Translation: AAH42134.1.
BC071873 mRNA. Translation: AAH71873.1.
AK074055 mRNA. Translation: BAB84881.1. Different initiation.
AK090430 mRNA. Translation: BAC03411.1.
AK095241 mRNA. Translation: BAC04506.1.
AB023228 mRNA. Translation: BAA76855.3.
AL080133 mRNA. Translation: CAB45729.1. Different initiation.
IPIIPI00239405.
IPI00239406.
IPI00239409.
IPI00239410.
IPI00239413.
IPI00239414.
IPI00412276.
IPI00815967.
IPI01009561.
PIRT12520.
T17215.
RefSeqNP_055995.4. NM_015180.4.
NP_878914.1. NM_182910.2.
NP_878917.1. NM_182913.2.
NP_878918.2. NM_182914.2.
UniGeneHs.525392.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DXSX-ray2.71B6857-6885[»]
4FI9X-ray3.05B6872-6885[»]
ProteinModelPortalQ8WXH0.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8WXH0. 5 interactions.

PTM databases

PhosphoSiteQ8WXH0.

Polymorphism databases

DMDM116242809.

Proteomic databases

PaxDbQ8WXH0.
PRIDEQ8WXH0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341472; ENSP00000344528; ENSG00000054654.
ENST00000344113; ENSP00000341781; ENSG00000054654.
ENST00000356081; ENSP00000348382; ENSG00000054654.
ENST00000357395; ENSP00000349969; ENSG00000054654.
ENST00000358025; ENSP00000350719; ENSG00000054654.
ENST00000394768; ENSP00000378249; ENSG00000054654.
ENST00000441438; ENSP00000396794; ENSG00000054654.
ENST00000458046; ENSP00000391937; ENSG00000054654.
ENST00000555002; ENSP00000450831; ENSG00000054654.
ENST00000555022; ENSP00000451009; ENSG00000054654.
GeneID23224.
KEGGhsa:23224.
UCSCuc001xgk.3. human.
uc001xgl.3. human.
uc001xgm.3. human.
uc001xgn.3. human.
uc001xgs.3. human.
uc001xgt.3. human.
uc010aqa.3. human.

Organism-specific databases

CTD23224.
GeneCardsGC14P064319.
HGNCHGNC:17084. SYNE2.
HPAHPA003435.
MIM608442. gene.
612999. phenotype.
neXtProtNX_Q8WXH0.
Orphanet98853. Autosomal dominant Emery-Dreifuss muscular dystrophy.
PharmGKBPA128394613.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
OMAEDWHKFI.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ8WXH0.
BgeeQ8WXH0.
GenevestigatorQ8WXH0.
GermOnlineENSG00000054654. Homo sapiens.

Family and domain databases

Gene3D1.10.418.10. 2 hits.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR012315. KASH.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamPF00307. CH. 2 hits.
PF10541. KASH. 1 hit.
PF00435. Spectrin. 3 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00150. SPEC. 18 hits.
[Graphical view]
SUPFAMSSF47576. Calponin-homology. 1 hit.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS51049. KASH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi23224.
NextBio44823.
SOURCESearch...

Entry information

Entry nameSYNE2_HUMAN
AccessionPrimary (citable) accession number: Q8WXH0
Secondary accession number(s): Q540G1 expand/collapse secondary AC list , Q8N1S3, Q8NF49, Q8TER7, Q8WWW3, Q8WWW4, Q8WWW5, Q8WXH1, Q9NU50, Q9UFQ4, Q9Y2L4, Q9Y4R1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: October 17, 2006
Last modified: May 1, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families